ABSTRACT
Angiogenesis is one of the essential processes that occur during wound healing. It is responsible for providing immunity as well as the regenerative cells, nutrition, and oxygen needed for the healing of the alveolar socket following tooth extraction. The inappropriate removal of formed blood clots causes the undesirable phenomenon of alveolar osteitis (AO) or dry socket. In this review, we aimed to investigate whether enhanced angiogenesis contributes to a more effective prevention of AO. The potential pro- or anti-angiogenic activity of different materials used for the treatment of AO were evaluated. An electronic search was performed in the PubMed, MEDLINE, and EMBASE databases via OVID from January 2000 to September 2016 using the keywords mentioned in the PubMed and MeSH (Medical Subject Headings) terms regarding the role of angiogenesis in the prevention of AO. Our initial search identified 408 articles using the keywords indicated above, with 38 of them meeting the inclusion criteria set for this review. Due to the undeniable role of angiogenesis in the socket healing process, it is beneficial if strategies for preventing AO are directed toward more proangiogenic materials and modalities.
Subject(s)
Dry Socket , Endothelial Cells , Oxygen , Regeneration , Tooth Extraction , Wound HealingABSTRACT
Recently, botulinum neurotoxin [BoNT]-derived recombinant proteins have been suggested as potential botulism vaccines. Here, with concentrating on BoNT type E [BoNT/E], we studied two of these binding domain-based recombinant proteins: a multivalent chimer protein, which is composed of BoNT serotypes A, B and E binding subdomains, and a monovalent recombinant protein, which contains 93 amino acid residues from recombinant C-terminal heavy chain of BoNT/E [rBoNT/E-HCC]. Both proteins have an identical region [48 aa] that contains one of the most important BoNT/E epitopes [YLTHMRD sequence]. The recombinant protein efficiency in antibody production, their structural differences, and their BoNT/E-epitope location were compared by using ELISA, circular dichroism, computational modeling, and hydrophobicity predictions. Immunological studies indicated that the antibody yield against rBoNT/E-HCC was higher than chimer protein. Cross ELISA confirmed that the antibodies against the chimer protein recognized rBoNT/E-HCC more efficiently. However, both antibody groups [anti-chimer and anti-rBoNT/E-HCC antibodies] were able to recognize other proteins. Structural studies with circular dichroism showed that chimer proteins have slightly more secondary structures than rBoNT/E-HCC. The immunological results suggested that the above-mentioned identical region in rBoNT/E-HCC is more exposed. Circular dichroism, computational protein modeling and hydrophobicity predictions indicated a more exposed location for the identical region in rBoNT/E-HCC than the chimer protein, which is strongly in agreement with immunological results